Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P48591 (RIR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase large subunit

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene names
Name:RnrL
ORF Names:CG5371
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small subunit.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 1 ATP-cone domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 812812Ribonucleoside-diphosphate reductase large subunit
PRO_0000187193

Regions

Domain12 – 10392ATP-cone
Region22 – 287Allosteric activator binding By similarity
Region228 – 2292Substrate binding By similarity
Region296 – 2994Allosteric effector binding, determines substrate specificity By similarity
Region438 – 4425Substrate binding By similarity
Region614 – 6185Substrate binding By similarity

Sites

Active site4381Proton acceptor By similarity
Active site4401Cysteine radical intermediate By similarity
Active site4421Proton acceptor By similarity
Binding site161Allosteric activator By similarity
Binding site641Allosteric activator By similarity
Binding site991Allosteric activator By similarity
Binding site2131Substrate By similarity
Binding site2581Substrate; via amide nitrogen By similarity
Site2291Important for hydrogen atom transfer By similarity
Site2371Allosteric effector binding, determines substrate specificity By similarity
Site2671Allosteric effector binding, determines substrate specificity By similarity
Site4551Important for hydrogen atom transfer By similarity
Site7481Important for electron transfer By similarity
Site7491Important for electron transfer By similarity
Site8071Interacts with thioredoxin/glutaredoxin By similarity
Site8101Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Modified residue7781Phosphothreonine Ref.5
Modified residue7821Phosphoserine Ref.5
Modified residue7861Phosphotyrosine Ref.5
Disulfide bond229 ↔ 455Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P48591 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 6E4FC608AC04A5FD

FASTA81291,978
        10         20         30         40         50         60 
MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI TLQVINGLYC 

        70         80         90        100        110        120 
GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE TKKAFSDVFE DLYNHVNKET 

       130        140        150        160        170        180 
NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR DFGYNYFGFK TLERSYLLKR NGKIAERPQH 

       190        200        210        220        230        240 
MLMRVAIGIH GEDIDAAVET YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE 

       250        260        270        280        290        300 
GIFKSVEQCA MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG 

       310        320        330        340        350        360 
GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM KRVEANGDWS 

       370        380        390        400        410        420 
LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL WFAIIEAQVE TGNPYMLFKD 

       430        440        450        460        470        480 
ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD EIAVCNLASI ALNMFVTPEK TYDFKKLKEV 

       490        500        510        520        530        540 
TKIVTKNLNK IIDINYYPLP EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ 

       550        560        570        580        590        600 
QIFETIYYGA LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR 

       610        620        630        640        650        660 
MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH HLLRDLTELD 

       670        680        690        700        710        720 
LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK STIKMAADRG AFIDQSQSFN 

       730        740        750        760        770        780 
IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE 

       790        800        810 
GSPQKYEEDR ERKMADMVCS LENKDACMSC GS 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila complementary DNA resource."
Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A.
Science 287:2222-2224(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"Developmental control of a G1-S transcriptional program in Drosophila."
Duronio R.J., O'Farrell P.H.
Development 120:1503-1515(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-343.
Strain: Oregon-R.
[5]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778; SER-782 AND TYR-786, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF52913.2.
AF132143 mRNA. Translation: AAD33590.1.
AY119149 mRNA. Translation: AAM51009.1.
U09369 Genomic DNA. Translation: AAA56995.1.
RefSeqNP_477027.1. NM_057679.5.
UniGeneDm.3216.

3D structure databases

ProteinModelPortalP48591.
SMRP48591. Positions 26-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60477. 3 interactions.
DIPDIP-19582N.
MINTMINT-829510.

Proteomic databases

PaxDbP48591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080059; FBpp0079648; FBgn0011703.
GeneID34392.
KEGGdme:Dmel_CG5371.

Organism-specific databases

CTD34392.
FlyBaseFBgn0011703. RnrL.

Phylogenomic databases

eggNOGCOG0209.
GeneTreeENSGT00390000001372.
InParanoidP48591.
KOK10807.
OMAEACLMCQ.
OrthoDBEOG7BGHK2.
PhylomeDBP48591.

Enzyme and pathway databases

UniPathwayUPA00326.

Gene expression databases

BgeeP48591.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34392.
NextBio788275.
PROP48591.

Entry information

Entry nameRIR1_DROME
AccessionPrimary (citable) accession number: P48591
Secondary accession number(s): Q9UB08, Q9VKZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase